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Literature summary extracted from

  • Wang, D.; Wang, C.; Wu, H.; Li, Z.; Ye, Q.
    Glutathione production by recombinant Escherichia coli expressing bifunctional glutathione synthetase (2016), J. Ind. Microbiol. Biotechnol., 43, 45-53 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.2 gene gshF, recombinant expression in Escherichia coli strain JM109 from plasmid pTrc99A Streptococcus thermophilus
6.3.2.3 gene gshF, recombinant expression in Escherichia coli strain JM109 from plasmid pTrc99A Streptococcus thermophilus

Protein Variants

EC Number Protein Variants Comment Organism
6.3.2.2 additional information a recombinant Escherichia coli strain expressing gshF encoding the bifunctional glutathione synthetase of Streptococcus thermophilus is constructed for efficient GSH production. The cultivation process is optimized by controlling dissolved oxygen, amino acid addition, and glucose feeding. 36.8 mM (11.3 g/l) GSH are formed at a productivity of 2.06 mM/h when the amino acid precursors (75 mM each) are added and glucose is supplied as the sole carbon and energy source. The fed-batch fermentations are performed in a 5-l bioreactor containing 2.5 l medium for fed-batch culture inoculated with 140 ml secondary seed culture. The temperature and pH are controlled at 37°C and 7.0, respectively. The GSH production is extremely limited by the precursors of GSH, and the GSH productivity is only 0.18 mM/h. Method evaluation, overview Streptococcus thermophilus
6.3.2.3 additional information a recombinant Escherichia coli strain expressing gshF encoding the bifunctional glutathione synthetase of Streptococcus thermophilus is constructed for efficient GSH production. The cultivation process is optimized by controlling dissolved oxygen, amino acid addition, and glucose feeding. 36.8 mM (11.3 g/l) GSH are formed at a productivity of 2.06 mM/h when the amino acid precursors (75 mM each) are added and glucose is supplied as the sole carbon and energy source. The fed-batch fermentations are performed in a 5-l bioreactor containing 2.5 l medium for fed-batch culture inoculated with 140 ml secondary seed culture. The temperature and pH are controlled at 37°C and 7.0, respectively. The GSH production is extremely limited by the precursors of GSH, and the GSH productivity is only 0.18 mM/h. Method evaluation, overview Streptococcus thermophilus

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.2 glutathione the L-glutamate L-cysteine ligase of enzyme gshF is feedback inhibited by GSH Streptococcus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.2 Mg2+ required Streptococcus thermophilus
6.3.2.3 Mg2+ required Streptococcus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.2 ATP + L-glutamate + L-cysteine Streptococcus thermophilus
-
 ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine Streptococcus thermophilus SIIM B218
-
 ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 additional information Streptococcus thermophilus the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 ?
-
 ?
6.3.2.2 additional information Streptococcus thermophilus SIIM B218 the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 ?
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine Streptococcus thermophilus
-
 ADP + phosphate + glutathione
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine Streptococcus thermophilus SIIM B218
-
 ADP + phosphate + glutathione
-
 ?
6.3.2.3 additional information Streptococcus thermophilus the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 ?
-
 ?
6.3.2.3 additional information Streptococcus thermophilus SIIM B218 the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.2 Streptococcus thermophilus D4N891
-
-
6.3.2.2 Streptococcus thermophilus SIIM B218 D4N891
-
-
6.3.2.3 Streptococcus thermophilus D4N891
-
-
6.3.2.3 Streptococcus thermophilus SIIM B218 D4N891
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Streptococcus thermophilus ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 ATP + L-glutamate + L-cysteine
-
 Streptococcus thermophilus SIIM B218 ADP + phosphate + gamma-L-glutamyl-L-cysteine
-
 ?
6.3.2.2 additional information the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 Streptococcus thermophilus ?
-
 ?
6.3.2.2 additional information the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 Streptococcus thermophilus SIIM B218 ?
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine
-
 Streptococcus thermophilus ADP + phosphate + glutathione
-
 ?
6.3.2.3 ATP + gamma-L-glutamyl-L-cysteine + glycine
-
 Streptococcus thermophilus SIIM B218 ADP + phosphate + glutathione
-
 ?
6.3.2.3 additional information the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 Streptococcus thermophilus ?
-
 ?
6.3.2.3 additional information the bifunctional enzyme GshF exhibits the activities of glutamate-cyseteine ligase, EC 6.3.2.2, and glutathione synthetase, EC 6.3.2.3 Streptococcus thermophilus SIIM B218 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.2.2 bifunctional glutathione synthetase
-
 Streptococcus thermophilus
6.3.2.2 bifunctional GSH synthetase
-
 Streptococcus thermophilus
6.3.2.2 gamma-GCS
-
 Streptococcus thermophilus
6.3.2.2 ghF
-
 Streptococcus thermophilus
6.3.2.2 GSH1
-
 Streptococcus thermophilus
6.3.2.2 gshAB gene name, UniProt Streptococcus thermophilus
6.3.2.2 GshF
-
 Streptococcus thermophilus
6.3.2.2 L-glutamate L-cysteine ligase
-
 Streptococcus thermophilus
6.3.2.2 More cf. EC 6.3.2.3 Streptococcus thermophilus
6.3.2.3 bifunctional glutathione synthetase
-
 Streptococcus thermophilus
6.3.2.3 bifunctional GSH synthetase
-
 Streptococcus thermophilus
6.3.2.3 ghF
-
 Streptococcus thermophilus
6.3.2.3 GSH2
-
 Streptococcus thermophilus
6.3.2.3 gshAB gene name, UniProt Streptococcus thermophilus
6.3.2.3 GshF
-
 Streptococcus thermophilus
6.3.2.3 L-glutathione synthetase
-
 Streptococcus thermophilus
6.3.2.3 More cf. Ec 6.3.2.2 Streptococcus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.2.2 30
-
 assay at Streptococcus thermophilus
6.3.2.3 30
-
 assay at Streptococcus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.2 8.5
-
 assay at Streptococcus thermophilus
6.3.2.3 8.5
-
 assay at Streptococcus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.2 ATP
-
 Streptococcus thermophilus
6.3.2.3 ATP
-
 Streptococcus thermophilus

General Information

EC Number General Information Comment Organism
6.3.2.2 metabolism the bifunctional enzyme gshF catalyzes both steps of glutathione biosynthesis in Streptococcus thermophilus Streptococcus thermophilus
6.3.2.2 physiological function the bifunctional GSH synthetase catalyzes two steps in GSH synthesis, which are usually catalyzed through L-glutamate L-cysteine ligase (gamma-GCS) and L-glutathione synthetase (GS) Streptococcus thermophilus
6.3.2.3 evolution the enzyme is a member of the ATP-grasp superfamily of enzymes Streptococcus thermophilus
6.3.2.3 metabolism the bifunctional enzyme gshF catalyzes both steps of glutathione biosynthesis in Streptococcus thermophilus Streptococcus thermophilus
6.3.2.3 physiological function the bifunctional GSH synthetase catalyzes two steps in GSH synthesis, which are usually catalyzed through L-glutamate L-cysteine ligase (gamma-GCS) and L-glutathione synthetase (GS) Streptococcus thermophilus